This purified mouse anti-ATP Synthase monoclonal antibody recognizes ATP synthase subunit beta. The epitope recognized by the anti-complex V-β subunit mAb 3D5AB1 is in the region containing the active site of the β-subunit and is centered approximately at amino acid residue 83. Anti-ATP Synthase Subunit Beta Monoclonal Antibody can be used in applications such as Western Blotting and Immunocytochemistry.

Antibody Specifications:

• Applications: Validated applications for anti-ATP Synthase Subunit Beta Monolconal Antibody are Western Blotting and Immunocytochemistry.
• Host Species and Isotype: The host species and isotype of the anti-ATP Synthase monoclonal antibody is mouse IgG1-κ.
• Clone ID of Monoclonal Antibody (mAb): The anti-ATP Synthase monoclonal antibody clone is 3D5AB1.
• Reactivity: Reacts with human, bovine, mouse, monkey, rat, and C. elegans.
• Product Size: Mouse anti-ATP Synthase Subunit Beta Monoclonal Antibody is lyophilized in a 100 µg pack size.

The epitope recognized by the anti-complex V-beta subunit mAb 3D5AB1 is in the region containing the active site of the β-subunit and is centered approximately at amino acid residue 83. Angiostatin-like activity of a monoclonal antibody to the catalytic subunit Complex V, also called F1F0ATPase or ATP synthase, is responsible for ATP production in oxidative phosphorylation and can work in reverse as a proton pumping ATPase. The enzyme was thought to be localized exclusively to mitochondria. However, it has recently been identified on the plasma membrane of several cell types including hepatocytes where it functions as the HDL receptor, on endothelial cells where it may act as the angiostatin receptor, and on the surface of cancer cells. The enzyme in mammals is composed of 17 subunits, five of which make up the easily detached F₁. The remainder subunits are components of two stalk domains and the proton pumping F₀ part of the machinery. Two of the subunits of the F₀ part are encoded on mitochondrial DNA while the other subunits are nuclear encoded. Mutations in the mitochondrial-encoded subunits of ATP synthase (Complex V) cause OXPHOS disease.